Journal ArticleDOI
γ-Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
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TLDR
Two homologous sulfur‐rich basic polypeptides form wheat endosperm, so‐called γ1‐Purothionin and γ2‐purothIONin, are described and present a high degree of homology among themselves and are the first two thionin‐like polypePTides, so-called y‐thionins, described from wheatendosperm.About:
This article is published in FEBS Letters.The article was published on 1990-09-17. It has received 214 citations till now. The article focuses on the topics: Endosperm & Amino acid.read more
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Plant Products as Antimicrobial Agents
TL;DR: The current status of botanical screening efforts, as well as in vivo studies of their effectiveness and toxicity, are summarized and the structure and antimicrobial properties of phytochemicals are addressed.
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Antimicrobial peptides: premises and promises.
TL;DR: Peptides, namely magainin and nisin have been shown to demonstrate contraceptive properties in vitro and in vivo and a few peptides have already entered clinical trials for the treatment of impetigo, diabetic foot ulcers and gastric helicobacter infections.
Journal ArticleDOI
Plant defensins: novel antimicrobial peptides as components of the host defense system.
TL;DR: A novel class of plant peptides whose structural and functional properties resemble those of insect and mammalian defensins are characterized, which are one class among the numerous types of Cys-rich antimicrobial peptides.
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Small cysteine-rich antifungal proteins from radish: their role in host defense.
Franky R. G. Terras,Kristel Eggermont,Kovaleva,Natasha V. Raikhel,Rupert W. Osborn,Kester A,Rees Sb,Sophie Torrekens,Van Leuven F,Jozef Vanderleyden +9 more
TL;DR: It is demonstrated that two homologous, 5-kD cysteine-rich proteins designated Raphanus sativus-antifungal protein 1 and Rs-AFP2 are located in the cell wall and occur predominantly in the outer cell layers lining different seed organs, and are preferentially released during seed germination after disruption of the seed coat.
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Plant pathogenesis-related (PR) proteins: a focus on PR peptides.
TL;DR: This review specifically focuses on these pathogenesis-related peptides, including proteinase inhibitors, plant defensins, thionins,Thionins and lipid transfer proteins, including novel peptide families, including PR-6 family, which are identified during the last decade.
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Thionins: Plant Peptides that Modify Membrane Permeability in Cultured Mammalian Cells
TL;DR: The results suggest that the inhibition of protein, RNA and DNA synthesis in BHK cells might be a consequence of membrane leakiness induced by thionin treatment.
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Primary structure of the hydrophobic plant protein crambin.
TL;DR: Methods to estimate protein secondary structure were applied and found to predict all of crambin's structure except its amphiphilic helix, and revealed that crambin is homologous with the plant toxins purothionin and viscotoxin.
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A toxic thionin from Pyrularia pubera: Purification, properties, and amino acid sequence
TL;DR: A low-molecular-weight cytotoxic protein has been purified from Pyrularia pubera Michx and is clearly a thionin, as shown by its close resemblance to the thionins from wheat and barley, to the viscotoxins from mistletoes, and to crambin.
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Complete primary structures of two subunits of purothionin A, a lethal protein for brewer's yeast from wheat flour.
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Amino Acid Sequence of a Purothionin Homolog from Barley Flour
Yasuhiko Ozaki,Keishiro Wada,Toshiharu Hase,Hiroshi Matsubara,Toshihiro Nakanishi,Hajime Yoshizumi +5 more
TL;DR: A purothionin homolog was isolated from barley flour and purified by CM-52 column chromatography and showed potent lethal activity towards brewer's yeast and its complete amino acid sequence was determined to be as follows.